2xg9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xg9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XG9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XG9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2xg9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XG9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XG9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xfy|2xfy]], [[2xff|2xff]], [[1b1y|1b1y]], [[2xfr|2xfr]], [[2xgb|2xgb]], [[2xgi|2xgi]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xfy|2xfy]], [[2xff|2xff]], [[1b1y|1b1y]], [[2xfr|2xfr]], [[2xgb|2xgb]], [[2xgi|2xgi]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xg9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xg9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xg9 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xg9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xg9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xg9 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Amylase|Amylase]] | *[[Amylase|Amylase]] | ||
*[[User:Gabriel Pons/Sandbox 2|User:Gabriel Pons/Sandbox 2]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Beta-amylase]] | [[Category: Beta-amylase]] | ||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Denyer, K | [[Category: Denyer, K]] | ||
[[Category: Field, R A | [[Category: Field, R A]] | ||
[[Category: Lawson, D M | [[Category: Lawson, D M]] | ||
[[Category: Naldrett, M J | [[Category: Naldrett, M J]] | ||
[[Category: Rejzek, M | [[Category: Rejzek, M]] | ||
[[Category: Smith, A M | [[Category: Smith, A M]] | ||
[[Category: Southard, A M | [[Category: Southard, A M]] | ||
[[Category: Stanley, D | [[Category: Stanley, D]] | ||
[[Category: Stevenson, C E.M | [[Category: Stevenson, C E.M]] | ||
[[Category: Carbohydrate metabolism]] | [[Category: Carbohydrate metabolism]] | ||
[[Category: Germination]] | [[Category: Germination]] | ||
Revision as of 13:58, 20 January 2015
Crystal structure of Barley Beta-Amylase complexed with 4-O-alpha-D- glucopyranosylmoranolineCrystal structure of Barley Beta-Amylase complexed with 4-O-alpha-D- glucopyranosylmoranoline
Structural highlights
Publication Abstract from PubMedThere are major issues regarding the proposed pathway for starch degradation in germinating cereal grain. Given the commercial importance but genetic intractability of the problem, we have embarked on a program of chemical genetics studies to identify and dissect the pathway and regulation of starch degradation in germinating barley grains. As a precursor to in vivo studies, here we report systematic analysis of the reversible and irreversible inhibition of the major beta-amylase of the grain endosperm (BMY1). The molecular basis of inhibitor action was defined through high resolution X-ray crystallography studies of unliganded barley beta-amylase, as well as its complexes with glycone site binder disaccharide iminosugar G1M, irreversible inhibitors alpha-epoxypropyl and alpha-epoxybutyl glucosides, which target the enzyme's catalytic residues, and the aglycone site binders acarbose and alpha-cyclodextrin. Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley beta-amylase.,Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA Mol Biosyst. 2010 Nov 18. PMID:21085740[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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